1Q17
Structure of the yeast Hst2 protein deacetylase in ternary complex with 2'-O-acetyl ADP ribose and histone peptide
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| A | 0051287 | molecular_function | NAD binding |
| A | 0070403 | molecular_function | NAD+ binding |
| B | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| B | 0051287 | molecular_function | NAD binding |
| B | 0070403 | molecular_function | NAD+ binding |
| C | 0017136 | molecular_function | histone deacetylase activity, NAD-dependent |
| C | 0051287 | molecular_function | NAD binding |
| C | 0070403 | molecular_function | NAD+ binding |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN A 401 |
| Chain | Residue |
| A | CYS143 |
| A | CYS146 |
| A | CYS170 |
| A | CYS173 |
| site_id | AC2 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN B 401 |
| Chain | Residue |
| B | CYS143 |
| B | CYS146 |
| B | CYS170 |
| B | CYS173 |
| site_id | AC3 |
| Number of Residues | 4 |
| Details | BINDING SITE FOR RESIDUE ZN C 401 |
| Chain | Residue |
| C | CYS146 |
| C | CYS170 |
| C | CYS173 |
| C | CYS143 |
| site_id | AC4 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL C 701 |
| Chain | Residue |
| C | ARG204 |
| C | ARG240 |
| site_id | AC5 |
| Number of Residues | 1 |
| Details | BINDING SITE FOR RESIDUE CL B 702 |
| Chain | Residue |
| B | TRP202 |
| site_id | AC6 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL A 703 |
| Chain | Residue |
| A | ARG204 |
| A | ARG240 |
| site_id | AC7 |
| Number of Residues | 2 |
| Details | BINDING SITE FOR RESIDUE CL B 704 |
| Chain | Residue |
| B | ARG204 |
| B | ARG240 |
| site_id | AC8 |
| Number of Residues | 23 |
| Details | BINDING SITE FOR RESIDUE APR A 1001 |
| Chain | Residue |
| A | GLY32 |
| A | ALA33 |
| A | GLY34 |
| A | THR37 |
| A | ASP43 |
| A | PHE44 |
| A | ARG45 |
| A | TYR52 |
| A | GLN115 |
| A | HIS135 |
| A | GLY223 |
| A | THR224 |
| A | SER225 |
| A | VAL228 |
| A | ASN248 |
| A | LEU249 |
| A | GLU250 |
| A | GLN268 |
| A | TYR269 |
| A | SER270 |
| A | HOH1003 |
| A | HOH1025 |
| A | HOH1041 |
| site_id | AC9 |
| Number of Residues | 24 |
| Details | BINDING SITE FOR RESIDUE APR B 1002 |
| Chain | Residue |
| B | GLY32 |
| B | ALA33 |
| B | GLY34 |
| B | THR37 |
| B | ASP43 |
| B | PHE44 |
| B | ARG45 |
| B | TYR52 |
| B | GLN115 |
| B | HIS135 |
| B | GLY223 |
| B | THR224 |
| B | SER225 |
| B | VAL228 |
| B | ASN248 |
| B | LEU249 |
| B | GLN268 |
| B | TYR269 |
| B | SER270 |
| B | HOH1007 |
| B | HOH1009 |
| B | HOH1023 |
| B | HOH1024 |
| B | HOH1046 |
| site_id | BC1 |
| Number of Residues | 20 |
| Details | BINDING SITE FOR RESIDUE APR C 1003 |
| Chain | Residue |
| C | GLY32 |
| C | ALA33 |
| C | GLY34 |
| C | THR37 |
| C | ASP43 |
| C | PHE44 |
| C | ARG45 |
| C | TYR52 |
| C | GLN115 |
| C | HIS135 |
| C | GLY223 |
| C | THR224 |
| C | SER225 |
| C | VAL228 |
| C | ASN248 |
| C | LEU249 |
| C | GLN268 |
| C | TYR269 |
| C | SER270 |
| C | HOH1022 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 3 |
| Details | Active site: {"description":"Proton acceptor","evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"20726530","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI2 |
| Number of Residues | 84 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI3 |
| Number of Residues | 12 |
| Details | Binding site: {"evidences":[{"source":"PROSITE-ProRule","id":"PRU00236","evidenceCode":"ECO:0000255"},{"source":"PubMed","id":"14502267","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"14604530","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"15150415","evidenceCode":"ECO:0000269"},{"source":"PubMed","id":"17289592","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
| site_id | SWS_FT_FI4 |
| Number of Residues | 3 |
| Details | Modified residue: {"description":"N-acetylserine","evidences":[{"source":"PubMed","id":"22814378","evidenceCode":"ECO:0007744"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 7 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| A | PRO42 | hydrogen bond acceptor, steric role |
| A | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
| A | PHE44 | steric role, van der waals interaction |
| A | ARG45 | electrostatic stabiliser, hydrogen bond donor |
| A | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
| A | ASP118 | activator, hydrogen bond acceptor |
| A | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA2 |
| Number of Residues | 7 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| B | PRO42 | hydrogen bond acceptor, steric role |
| B | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
| B | PHE44 | steric role, van der waals interaction |
| B | ARG45 | electrostatic stabiliser, hydrogen bond donor |
| B | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
| B | ASP118 | activator, hydrogen bond acceptor |
| B | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
| site_id | MCSA3 |
| Number of Residues | 7 |
| Details | M-CSA 240 |
| Chain | Residue | Details |
| C | PRO42 | hydrogen bond acceptor, steric role |
| C | ASP43 | hydrogen bond acceptor, hydrogen bond donor, steric role |
| C | PHE44 | steric role, van der waals interaction |
| C | ARG45 | electrostatic stabiliser, hydrogen bond donor |
| C | ASN116 | activator, electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase nucleophilicity |
| C | ASP118 | activator, hydrogen bond acceptor |
| C | HIS135 | hydrogen bond acceptor, hydrogen bond donor, proton acceptor, proton donor |
